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BST2 bone marrow stromal cell antigen 2 [ Homo sapiens (human) ]

Gene ID: 684, updated on 12-May-2015
Official Symbol
BST2provided by HGNC
Official Full Name
bone marrow stromal cell antigen 2provided by HGNC
Primary source
HGNC:HGNC:1119
See related
Ensembl:ENSG00000130303; HPRD:02759; MIM:600534; Vega:OTTHUMG00000165993
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
CD317; TETHERIN
Summary
Bone marrow stromal cells are involved in the growth and development of B-cells. The specific function of the protein encoded by the bone marrow stromal cell antigen 2 is undetermined; however, this protein may play a role in pre-B-cell growth and in rheumatoid arthritis. [provided by RefSeq, Jul 2008]
Orthologs
See BST2 in MapViewer
Location:
19p13.1
Exon count:
5
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 19 NC_000019.10 (17402939..17405648, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 19 NC_000019.9 (17502238..17516458, complement)

Chromosome 19 - NC_000019.10Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105372298 Neighboring gene uncharacterized LOC105372343 Neighboring gene multivesicular body subunit 12A Neighboring gene BST2 interferon stimulated positive regulator (non-protein coding) Neighboring gene high mobility group box 3 pseudogene 29

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Replication interactions

Interaction Pubs
Knockdown of BST-2 by siRNA enhances production of infectious HIV-1 particles in HeLa cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp160, precursor env BST-2 co-localizes with HIV-1 Env at the virological synapse on infected T cells PubMed
Nef nef HIV-1 group O Nefs downregulate the longer form of human tetherin but not the shorter form PubMed
nef Mutation of the four residues (K186V, Q188R, S192A, and L195T) in HIV-1 group O Nefs significantly reduces Nef-mediated downregulation of human tetherin PubMed
nef HIV-1 group O Nefs evolve the ability to downregulate surface levels of tetherin and sequester it to intracellular perinuclear compartments PubMed
nef Residues I163 and C169 of HIV-1 Nef from chimpanzee-adapted HIV-1 JC16 are specifically involved in its interaction with tetherin PubMed
nef Tetherin upregulation in HIV-1-infected macrophages is HIV-1 Nef dependent, not a direct consequence of type I interferon induction PubMed
nef HIV-1 replication in immature dendritic cells upregulates tetherin independently of Vpu, but in a Nef-dependent manner PubMed
Pr55(Gag) gag BST-2 delays processing of cellular membrane-associated Gag proteins and adversely affects formation of the core structure in HIV-1 particles PubMed
gag In cells expressing either wild-type or vpu(-) virus, BST-2 and HIV-1 Gag co-localize both along the plasma membrane and in endosomes PubMed
gag The interaction between HIV-1 Gag and TSG101 enhances tetherin recruitment in HeLa cells. Both TSG101 and ALIX binding sites within the p6 domain of Gag enhance tetherin recruitment to Gag assembly sites in T cells PubMed
gag Tetherin potently inhibits release of Fyn(10)fullMA-Gag, which contains the first 10 amino acids of Fyn kinase at the N terminus of Gag, under cholesterol-depleting conditions in HeLa and HT-1080 cells PubMed
gag Tetherin co-localizes with HIV-1 Gag in CD81- and CD63-enriched intracellular virus-containing compartments in macrophages, and that a separate population of tetherin is located in the TGN PubMed
gag Tetherin accumulates with Gag at the contact zone between infected and target cells, but does not prevent the formation of virological synapses PubMed
gag Cell-free virus particles produced from BST-2 and HIV-1(Vpu-) cotransfected 293T cells have a significant accumulation of the pr55Gag precursor and the p40Gag intermediate products, leading to diminish the infectivity of HIV-1 particles PubMed
Tat tat HIV-1 and the viral protein Tat modulate the expression of bone marrow stromal cell antigen 2 (BST2) in immature dendritic cells and monocyte-derived macrophages PubMed
Vpr vpr HIV-1 Vpr downregulates BST2 expression in human glial cells PubMed
Vpu vpu HIV-1 Vpu stabilizes human tetherin in African green monkey kidney COS cells and still counteracts the ability of tetherin to suppress virus release PubMed
vpu Expression of HIV-1 Vpu induces co-localization of tetherin with early endosome protein EEA-1 or late endosome protein LAMP-1 PubMed
vpu The ability of HIV-1 Vpu to antagonize tetherin is important for the antibody opsonization of HIV-infected cells, which in turn increases FCGRIII (CD16) signaling PubMed
vpu RNAi-knockdown of tetherin, but not CD4 or NTB-A, increases the resistance of HIV-infected cells to antibody-dependent cell-mediated cytotoxicity (ADCC), suggesting Vpu protects infected cells from ADCC as a function of its ability to counteract tetherin PubMed
vpu HIV-1 Vpu counteracts the Tetherin-induced retention of HIV-1(delVpu) virion particles. Vpu colocalizes with Tetherin in co-expression cells PubMed
vpu HIV-1 Vpu downregulates BST-2. The transmembrane/ion channel domain and conserved serines in the cytoplasmic domain of Vpu are required for the Vpu-mediated downregulation of BST-2 PubMed
vpu N-terminally deleted BST-2 inhibits HIV-1 Vpu-defective and wild-type HIV-1 particle release, and the BST-2 mutant impairs its activity to activate NF-kappaB activation PubMed
vpu The 59EXXXLV64 motif in HIV-1 Vpu is required for Vpu-mediated tetherin downregulation. Vpu E/L/V mutant fails to downregulate tetherin but still interact with beta-TrCP2 and HRS (ESCRT-0) PubMed
vpu Vpu requires a functional polyubiquitin/proteasome system for efficient tetherin degradation. K48R ubiquitin mutant partially blocks Vpu-mediated tetherin downregulation PubMed
vpu HIV-1 Vpu proteins from nonpandemic HIV-1 O and P strains are poor mediators of human tetherin downregulation. Vpus from nonpandemic HIV-1 N strains are as good tetherin antagonists as those from pandemic HIV-1 M strains PubMed
vpu HIV-1 Vpu transmembrane mutants A14N and A18N do not support virus release in the presence of CD317, suggesting that Ala residues at position 14 and 18 are required to antagonize CD317 PubMed
vpu Vpu interferes with tetherin trafficking to the cell-surface and causes a relocalization of the cellular tetherin with a TGN marker TGN46 in the TGN, suggesting Vpu-mediated antagonism of tetherin involves binding and sequestration of tetherin in the TGN PubMed
vpu The plasma membrane clathrin adaptor protein complex AP-2 (mu2) is required for optimal downregulation of cell surface BST-2 by Vpu PubMed
vpu HIV-1 Vpu interacts with BST-2 in the trans-Golgi network or in early endosomes, leading to lysosomal degradation of BST-2. Vpu-mediated downregulation of BST-2 depends on cellular ubiquitination machinery via betaTrCP PubMed
vpu All three major structural domains (amino-terminal cytoplasmic tail, transmembrane domain, and extracellular coiled-coil domain) of BST-2 are involved in Vpu-mediated antagonism of tetherin PubMed
vpu The residues including 22 to 24 and 34 to 42 of tetherin play a crucial role in the Vpu interaction. I34, L37, and L41 of tetherin are involved in the determination of Vpu susceptibility PubMed
vpu HIV-1 group N Vpu from Togo downregulates both tetherin isoforms. HIV-2 Env, SIVmac Nef, and KSHV K5 target tetherin isoforms with equal efficiency PubMed
vpu Biotinylation technique in living cells demonstrates that HIV-1 Vpu-induced ER-to-cytosol retro-translocation of tetherin is first exposed to the cytosol as a dimeric oxidized complex and then becomes deglycosylated and reduces to monomers PubMed
vpu HIV-1 Vpu mutations (A19E, E29K, II43,46SL, R49G/T, SN53,55RH, S53N, E58K) derived from HIV-1 infected patients have defects for both CD4 and tetherin downregulation PubMed
vpu Individual Vpu proteins isolated from chronically or acutely infected patients differ substantially in their CD4 and tetherin downregulation function at the cell surface PubMed
vpu BiFC assay demonstrates that the cytoplasmic domain (CD) of HIV-1 Vpu physically interacts with both human and rhesus tetherins. The (G/D)DIWK motif in the CD of rhesus tetherin is responsible for the interaction and the functional antagonism by Vpu PubMed
vpu HIV-1 Vpu-mediated BST-2 downregulation is critical for HIV-1 replication and propagation in vivo in a beta-TrCP dependent manner, especially at early times post-infection PubMed
vpu The peptide BST2-TM-P1 competes with BST-2 binding to HIV-1 Vpu, resulting in restoration of the BST-2 level at HeLa-Vpu cell surface PubMed
vpu Rhesus BST2 inhibits the release of HIV-1 from cells and is resistant to HIV-1 Vpu. Transfer of residues 30-45 of human BST2 into rhesus BST2 is sufficient to confer sensitivity to Vpu PubMed
vpu HIV-1 Vpu interacts with CD317 via its transmembrane region (amino acids 4-27) in living cells PubMed
vpu Alternative translation initiation produces two isoforms of tetherin, l-isoform and s-isoform, which restrict HIV-1 (Vpu-) particle release, but only l-isoform is sentitive to counteraction by Vpu PubMed
vpu Human-monkey tetherin chimeras reveal that the transmembrane domains (amino acids I33V, I36L, P40L, and T45I) of tetherin are determinants of sensitivity/resistance to Vpu PubMed
vpu The betaTrCP binding motif DSGxxS of Vpu is required for optimal downregulation of BST-2 and enhancement of virion-release. Vpu serine (S52/S56) mutants are severely impaired for their ability to counteract tetherin antiviral activity PubMed
vpu The cytoplasmic tail of HIV-1 Vpu, specifically within the cytoplasmic tail hinge region (amino acids 47-60), are required for downregulation of both human tetherin and gibbon ape leukemia virus envelope (GaLV Env) PubMed
vpu Chimeras between the TMD of HIV-1 M Vpu and the cytoplasmic domains of SIVcpzPtt, SIVcpzPts, and SIVgor Vpu proteins are capable of counteracting human tetherin to enhance virion release PubMed
vpu The C-terminal alpha-helix (H2) of HIV-1 Vpu cytoplasmic tail domain (CTD) is sufficient to remove tetherin from sites of viral assembly and is necessary for full tetherin antagonist activity PubMed
vpu The residues Q2, P3, I4, A7, V20, V21, V25, I26, and I27 of the TM domain in HIV-1 Vpu form crosslinks with the residues LLL22-4, G27, I28, L29, P40, L41, I43, F44, T45, and I46 of the TM domain in tetherin PubMed
vpu Tetherin is in lipid rafts at the cell surface. Expression of HIV-1 Vpu relocalizes tetherin from the lipid rafts to intracellular endosome and lysosome compartments PubMed
vpu Amino acid substitution variants of tetherin (Y8H, R19H, N49S, D103N, E117A, D129E and V146L) in human populations maintain its ability to restrict virion release but do not confer resistance to HIV-1 Vpu or SIVtan Env PubMed
vpu HIV-1 Vpu proteins from Cameroonian group N viruses are largely unable to downregulate tetherin. Four amino acid substitutions (E15A, V19A and IV25/26LL) in the transmembrane domain of N-Vpu allow efficient interaction with human tetherin PubMed
vpu HIV-1 Vpu inhibits endogenous expression BST2-induced NF-kappaB activity in cells, and the inhibition requires the beta-TrCP binding motif (residues 51-56; DSGxxS) in Vpu PubMed
vpu HIV-1 Vpu variants from the group C show moderate virus release activity in comparison to group B Vpu variants. The TM domain from the inactive Vpu C is responsible for a significant decrease in egress activity and BST-2 downregulation PubMed
vpu A combination of molecular dynamics simulations and docking approaches shows the lowest energy structure of Vpu-BST2, indicating that Leu-11/14/19/23 and Ile-10/15/18 in BST2 interact with the alanine rim (Ala-8/11/15/19) of Vpu PubMed
vpu Analysis of the chimera HIV-1 Vpu proteins from group M and O shows that alanine-18 is important for group M Vpu localization and tetherin-Vpu interaction PubMed
vpu Overexpression of BST2 and downregulation of HIV-1 Vpu in HIV-1 infected TZM-bl cells inhibit HIV-1 replication PubMed
vpu The retention of HIV-1 Vpu from group O in ER-associated compartments confers a defect to antagonism even when interaction with tetherin is mediated through a chimeric TM domain PubMed
vpu Tetherin delGPI mutant directly interacts with HIV-1 Vpu and inhibits Vpu-induced degradation of tetherin and CD4. Transient expression of tetherin delGPI mutant also inhibits infectious HIV-1 release in tetherin-positive cells PubMed
vpu HIV-1 Vpu downregulates cell-surface BST-2 levels without qualitatively affecting the distribution of the restriction factor at the plasma membrane in HIV-1-infected Jurkat cells PubMed
vpu SCYL2 inhibits Vpu-induced BST2 and CD4 reduction at the cell surface by suppressing the phosphorylation of Vpu at positions Ser-52 and Ser-56 PubMed
vpu HIV-1 Vpu from chimpanzee-adapted HIV-1 JC16 downregulates both human and chimpanzee tetherin proteins as efficiently as that of HIV-1 NL4-3 Vpu PubMed
vpu Alanine-scanning mutagenesis and Ala-to-Leu replacement through the HIV-1 Vpu transmembrane domain (residues 5-28) reveals A14 and W22 are required for tetherin antagonism PubMed
vpu HIV-1 BF recombinant Vpu is associated with increased viral particle production when compared to WT B variant virus in tetherin-expressing cell lines PubMed
vpu HIV-1 Vpu rescues the decreased production of infectious HIV-1 virions and restores the diminished reverse transcriptase activities of the culture supernatants as a result of BST-2 inhibition PubMed
vpu Lysine residues (K18/K21) in tetherin are determinants for Vpu-mediated depletion of tetherin. This depletion, however, is dispenable for potent antagonism of the tetherin-mediated restriction of HIV-1 particle release PubMed
vpu A functional ER-associated degradation pathway is required for Vpu-induced tetherin degradation. P97 ATPase (VCP) knockdown partially impairs Vpu-mediated tetherin degradation PubMed
vpu Tetherin cytoplasmic tail lysine residues (K18 and K21) are ubiquitinated in the presence of HIV-1 Vpu and KSHV K5 PubMed
vpu HIV-1 Vpu transmembrane domain mutants V9D and I19D fail to promote HIV-1 virion release and to downregulate cell surface tetherin PubMed
vpu Mutation of a single amino acid (T45I) in the transmembrane region of BST-2 results in insensitivity to HIV-1 Vpu while maintaining antiviral activity PubMed
vpu HIV-1 Vpu co-immunoprecipitates with BST-2 in HEK293T cells and in HeLa Tet-Off cells. Deletion of two leucine residues at positions 22 and 23 in tetherin diminishes its association with Vpu PubMed
vpu HIV-1 Vpu reduces steady-state expression of BST-2 in transfected HeLa cells and in HIV-infected macrophages, but not in HIV-infected CEMx174 and H9 cells PubMed
vpu HIV-1 Vpu-A18H downregulates the expression of BST-2 at the cell surface and enhances virion release inefficiently through a reduced interaction with BST-2 PubMed
vpu Tetherin inhibits influenza virus neuraminidase (NA) virus-like particle (VLP) release, which is antagonized by HIV-1 Vpu PubMed
vpu In HIV-1-producing cells, CD317 relocalizes predominantly to TfR-positive recycling endosomes, to EEA1-postive early endosomes, and to gin97-positive trans-Golgi network compartments, with some present on late endocytic structures PubMed
vpu All potential acceptor sites (Ser3, Thr4, Ser5, Cys9, Lys18, Cys20, and Lys21) in the cytoplasmic domain of BST2 contribute to Vpu-induced ubiquitination PubMed
vpu BIT225, HIV-1 Vpu viroporin inhibitor, does not affect Vpu-tetherin interactions PubMed
vpu Reduced HIV-1 release in Rab7A-depleted cells is related to expression of the restriction factor tetherin, suggesting that Rab7A contributes to the mechanism by which Vpu counteracts tetherin and rescues HIV-1 release PubMed
vpu SHIV Vpu proteins can counteract human and rhesus BST-2 PubMed
vpu A computer modeling method predicts that the interface is composed of Vpu residues I6, A10, A14, A18, V25 and W22, and BST-2 residues L23, I26, V30, I34, V35, L41, I42, and T45 PubMed
vpu Endogenous tetherin cell surface expression in T-cell lines H9, CEM-CCRF and CEM-SS are different and that affects HIV-1 Vpu-mediated tetherin modulation on virus release PubMed
vpu An N-terminal deletion and T45I substitution in the TMD of human tetherin render the protein unresponsive to antagonism by HIV-1 Vpu PubMed
vpu NMR studies reveal that the 10AXXXAXXXAXXXW22 face of the Vpu transmembrane domain (TMD) directly binds to the large hydrophobic residues (aa 22-47) of the tetherin TMD in an anti-parallel manner PubMed
vpu The C-terminal fragment of the clathrin assembly protein AP180 inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env PubMed
vpu Dominant negative dynamin 2 (K44A) acts as an inhibitor of clathrin-mediated endocytosis and that it inhibits the downregulation of BST-2 from the cell surface by HIV-1 Vpu and HIV-2 Env PubMed
vpu The putative cholesterol recognition amino acid consensus (CRAC) motif (residues 25-31) of HIV-1 Vpu mediates lipid raft association of Vpu, but is dispensable for the downregulation of cell surface BST-2 PubMed
vpu Tetherin expression is upregulated following HIV-1 infection of monocytes-derived macrophages and is not fully downregulated by HIV-1 Vpu PubMed
vpu HIV-1 Vpu partially antagonizes the restriction of BST2 on HCV production and release from BST2 expressing Huh7.5 cells PubMed
vpu Downregulation of CD4 and BST2 by HIV-1 Vpu is observed in HIV-1 infected humanized mice PubMed
vpu P40L/T45I mutations in human tetherin leads to drastically decreased susceptibility of the mutant to HIV-1 Vpu, while susceptibility to SIVden Vpu increases to 50%, suggesting that these two residues participate in the species-specific activity of Vpu PubMed
vpu Overexpression of clathrin coat-associated protein AP180 inhibits Vpu-mediated tetherin antagonism but adaptor protein-1, adaptor protein-2, and adaptor protein-3 are dispensable PubMed
vpu HIV-1 Vpu E/L/V mutants interact with tetherin in infected cells and are incorporated into nascent virions in a tetherin-dependent manner PubMed
vpu Mutation of the 59EXXXLV64 motif in HIV-1 Vpu leads to endosomal and surface localization of Vpu and modulates the trafficking of tetherin PubMed
vpu The ubiquitin associated protein 1 (UBAP1)-containing ESCRT-I is essential for degradation of antiviral cell-surface protein such as tetherin (BST-2/CD317) by HIV-1 Vpu PubMed
vpu IFNalpha/ribavirin treatment in vivo induces APOBEC3G, APOBEC3F, and BST-2 expression and results in hyper-mutations in viral genome and A11G/S61A mutations in HIV-1 Vpu. These two mutations in Vpu enhances the interaction between BST-2 and Vpu PubMed
vpu Cholesterol-binding compound amphotericin B methyl ester (AME) inhibits the ability of HIV-1 Vpu to counteract the activity of CD317/BST-2/tetherin PubMed
vpu Deletion of amino acids leucine's 22/23 in BST-2 significantly diminishes its association with Vpu, leading to its resistance to antagonism by Vpu PubMed
vpu Monomeric tetherin and non-glycosylated tetherin are expressed at the cell surface and are sensitive to Vpu-induced downregulation PubMed
vpu HIV-1 Vpu antagonizes the effects of BCA2 on HIV-1 particle production in "tetherin-positive" cells PubMed
vpu HIV-1 Vpu and beta-TrCP co-immunoprecipitate with tetherin PubMed
vpu The v-ATPase VPS4 is required for Vpu-induced cell surface downregulation of BST-2 PubMed
vpu HRS interacts with both HIV-1 Vpu and tetherin by co-precipitation analysis PubMed
vpu HRS, an ESCRT-0 complex component, is required for the Vpu-induced downregulation of BST-2, indicating that Vpu-induced BST-2 degradation involves the ESCRT/MVB pathway PubMed
vpu Co-depletion of beta-TrCP1 and beta-TrCP2 support Vpu's activity to enhance virus release and to downregulate endogenous tetherin in TZM-bl cells PubMed
vpu The STS sequence in the cytoplasmic domain of BST2 is required for optimal Vpu-mediated downregulation of BST2 from the cell surface and the counteraction of virion release by Vpu PubMed
vpu HIV-1 Vpu accelerates the turnover of mature endogenous BST-2 in both HeLa and CEMx174 cells. The interference of Vpu with the newly synthesized BST-2 results in the gradual depletion of cell surface BST-2 PubMed
vpu CD317 exhibits a fast recycling kinetic that is sensitive to treatment with primaquine, a strong recycling inhibitor. HIV-1 Vpu interferes with the recycling of CD317 PubMed
vpu HIV-1 Vpu ion channel mutant S23A binds and antagonizes CD317, indicating that its ion channel function is not correlated with its ability to downregulate cell surface CD317 PubMed
vpu HIV-1 Vpu cytoplasmic domain mutants S56G and E59K fail to enhance HIV-1 virion release but can reduce cell surface tetherin, suggesting that downregulation of cell surface tetherin and enhancement of virion release by Vpu are not always correlated PubMed
capsid gag HIV-1 CA mutations, P99A and EE75,76AA, pair in tetherin recruitment to HIV-1 assembly sites PubMed

Go to the HIV-1, Human Interaction Database

  • Cytokine Signaling in Immune system, organism-specific biosystem (from REACTOME)
    Cytokine Signaling in Immune system, organism-specific biosystemCytokines are small proteins that regulate and mediate immunity, inflammation, and hematopoiesis. They are secreted in response to immune stimuli, and usually act briefly, locally, at very low concen...
  • Immune System, organism-specific biosystem (from REACTOME)
    Immune System, organism-specific biosystemHumans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first crit...
  • Interferon Signaling, organism-specific biosystem (from REACTOME)
    Interferon Signaling, organism-specific biosystemInterferons (IFNs) are cytokines that play a central role in initiating immune responses, especially antiviral and antitumor effects. There are three types of IFNs:Type I (IFN-alpha, -beta and others...
  • Interferon alpha/beta signaling, organism-specific biosystem (from REACTOME)
    Interferon alpha/beta signaling, organism-specific biosystemType I interferons (IFNs) are composed of various genes including IFN alpha (IFNA), beta (IFNB), omega, epsilon, and kappa. In humans the IFNA genes are composed of more than 13 subfamily genes, wher...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
metalloendopeptidase inhibitor activity IDA
Inferred from Direct Assay
more info
PubMed 
poly(A) RNA binding IDA
Inferred from Direct Assay
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein homodimerization activity IPI
Inferred from Physical Interaction
more info
PubMed 
signal transducer activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
Process Evidence Code Pubs
B cell activation IEA
Inferred from Electronic Annotation
more info
 
cell proliferation TAS
Traceable Author Statement
more info
PubMed 
cell-cell signaling TAS
Traceable Author Statement
more info
PubMed 
cytokine-mediated signaling pathway TAS
Traceable Author Statement
more info
 
defense response to virus IDA
Inferred from Direct Assay
more info
PubMed 
humoral immune response TAS
Traceable Author Statement
more info
PubMed 
innate immune response IDA
Inferred from Direct Assay
more info
PubMed 
multicellular organismal development TAS
Traceable Author Statement
more info
PubMed 
negative regulation of cell growth IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of cell migration IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of endopeptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of intracellular transport of viral material IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of plasmacytoid dendritic cell cytokine production IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of viral genome replication IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of I-kappaB kinase/NF-kappaB signaling IMP
Inferred from Mutant Phenotype
more info
PubMed 
regulation of actin cytoskeleton organization ISS
Inferred from Sequence or Structural Similarity
more info
 
response to interferon-alpha ISS
Inferred from Sequence or Structural Similarity
more info
 
response to interferon-beta ISS
Inferred from Sequence or Structural Similarity
more info
 
response to interferon-gamma ISS
Inferred from Sequence or Structural Similarity
more info
 
response to virus IDA
Inferred from Direct Assay
more info
PubMed 
type I interferon signaling pathway TAS
Traceable Author Statement
more info
 
Component Evidence Code Pubs
Golgi apparatus IDA
Inferred from Direct Assay
more info
 
anchored component of membrane IEA
Inferred from Electronic Annotation
more info
 
apical plasma membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
cell surface IMP
Inferred from Mutant Phenotype
more info
PubMed 
cell surface ISS
Inferred from Sequence or Structural Similarity
more info
 
cytoplasm IDA
Inferred from Direct Assay
more info
 
colocalizes_with cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
extracellular exosome IDA
Inferred from Direct Assay
more info
PubMed 
extracellular exosome TAS
Traceable Author Statement
more info
 
integral component of plasma membrane TAS
Traceable Author Statement
more info
PubMed 
membrane IDA
Inferred from Direct Assay
more info
PubMed 
membrane raft IEA
Inferred from Electronic Annotation
more info
 
multivesicular body IMP
Inferred from Mutant Phenotype
more info
PubMed 
plasma membrane IDA
Inferred from Direct Assay
more info
 
Preferred Names
bone marrow stromal antigen 2
Names
bone marrow stromal antigen 2
BST-2
HM1.24 antigen
NPC-A-7

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_004335.3NP_004326.1  bone marrow stromal antigen 2 precursor

    See identical proteins and their annotated locations for NP_004326.1

    Status: REVIEWED

    Source sequence(s)
    AI077344, BC033873, CB047887
    Consensus CDS
    CCDS12358.1
    UniProtKB/TrEMBL
    A0A024R7H5
    UniProtKB/Swiss-Prot
    Q10589
    Related
    ENSP00000252593, OTTHUMP00000231653, ENST00000252593, OTTHUMT00000387346
    Conserved Domains (1) summary
    TIGR02168
    Location:70152
    SMC_prok_B; chromosome segregation protein SMC, common bacterial type

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000019.10 Reference GRCh38.p2 Primary Assembly

    Range
    17402939..17405648
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018930.2 Alternate CHM1_1.1

    Range
    17513248..17515966
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)